Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.3.3 - coproporphyrinogen oxidase and Organism(s) Synechocystis sp. and UniProt Accession P72848

for references in articles please use BRENDA:EC1.3.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.3 coproporphyrinogen oxidase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Synechocystis sp.
UNIPROT: P72848 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
coproporphyrinogen oxidase, coproporphyrinogen iii oxidase, hem13, cpox4, copro'gen oxidase, coprogen oxidase, klhem13, oxygen-dependent coproporphyrinogen iii oxidase, hemn1, coproporphyrinogen-iii oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coproporphyrinogen III oxidase
-
CPgen oxidase
-
Coprogen oxidase
-
-
-
-
coproporphyrinogen III oxidase
coproporphyrinogenase
-
-
-
-
COX
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9076-84-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
is added to the assay at 10 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
CPO catalyzes the oxidative decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX in heme biosynthesis and is shared in chlorophyll biosynthesis in photosynthetic organisms. HemF plays an essential role under aerobic growth the photosynthetic organism, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40300
x * 40300, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40300, calculated from amino acid sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant terminally Strep-tagged HemF from Escherichia coli to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sll1185, overexpression of N-terminally Strep-tagged HemF in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goto, T.; Aoki, R.; Minamizaki, K.; Fujita, Y.
Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803
Plant Cell Physiol.
51
650-663
2010
Synechocystis sp., Synechocystis sp. (P72848)
Manually annotated by BRENDA team